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Proteintech cleaved caspase 3 immunofluorescence
$TMZ+TTF treatment enhances apoptotic responses in glioblastoma cells. (A) Immunofluorescence staining of <t>cleaved</t> <t>caspase‐3</t> (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under different treatment conditions. (B) Quantification of cleaved caspase‐3 fluorescence intensity. (C, E) Representative Annexin V‐FITC/PI flow cytometry plots showing the distribution of viable and apoptotic cell populations at 24 and 48 h in U251 and SHG140 cells, respectively. Lower left: Viable cells; lower right: Early apoptotic cells; upper right: Late apoptotic cells; upper left: PI‐positive non‐apoptotic/dead cells. (D, F) Quantitative analysis of viable‐cell fractions derived from Annexin V‐FITC/PI flow cytometry in U251 and SHG140 cells at 24 and 48 h. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. At least 10,000 events were acquired per flow‐cytometry sample. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test within each time point. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.$
Cleaved Caspase 3 Immunofluorescence, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 4864 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/caspase+3/Caspase+3%2Fp17%2Fp19+Antibody/pmc13651720-64-1-28
Average 97 stars, based on 4864 article reviews

cleaved caspase 3 immunofluorescence - by Bioz Stars, 2026-10

97/100 stars

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1) Product Images from "Tumor Treating Fields Enhance Temozolomide‐Associated Growth Suppression in Glioblastoma Cells and Patient‐Derived Organoids Through Cell‐Cycle Blockade, Apoptosis, and SMAD ‐Associated Signaling"

Article Title: Tumor Treating Fields Enhance Temozolomide‐Associated Growth Suppression in Glioblastoma Cells and Patient‐Derived Organoids Through Cell‐Cycle Blockade, Apoptosis, and SMAD ‐Associated Signaling

Journal: CNS Neuroscience & Therapeutics

doi: 10.1002/cns.71195

$TMZ+TTF treatment enhances apoptotic responses in glioblastoma cells. (A) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under different treatment conditions. (B) Quantification of cleaved caspase‐3 fluorescence intensity. (C, E) Representative Annexin V‐FITC/PI flow cytometry plots showing the distribution of viable and apoptotic cell populations at 24 and 48 h in U251 and SHG140 cells, respectively. Lower left: Viable cells; lower right: Early apoptotic cells; upper right: Late apoptotic cells; upper left: PI‐positive non‐apoptotic/dead cells. (D, F) Quantitative analysis of viable‐cell fractions derived from Annexin V‐FITC/PI flow cytometry in U251 and SHG140 cells at 24 and 48 h. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. At least 10,000 events were acquired per flow‐cytometry sample. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test within each time point. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.$
Figure Legend Snippet: TMZ+TTF treatment enhances apoptotic responses in glioblastoma cells. (A) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under different treatment conditions. (B) Quantification of cleaved caspase‐3 fluorescence intensity. (C, E) Representative Annexin V‐FITC/PI flow cytometry plots showing the distribution of viable and apoptotic cell populations at 24 and 48 h in U251 and SHG140 cells, respectively. Lower left: Viable cells; lower right: Early apoptotic cells; upper right: Late apoptotic cells; upper left: PI‐positive non‐apoptotic/dead cells. (D, F) Quantitative analysis of viable‐cell fractions derived from Annexin V‐FITC/PI flow cytometry in U251 and SHG140 cells at 24 and 48 h. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. At least 10,000 events were acquired per flow‐cytometry sample. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test within each time point. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Techniques Used: Immunofluorescence, Staining, Fluorescence, Flow Cytometry, Analysis, Derivative Assay

ALK5/TGFβRI inhibition partially attenuates TTF‐associated SMAD phosphorylation, growth suppression, and cleaved caspase‐3 induction. (A) Western blot analysis of phosphorylated SMAD2 (p‐SMAD2), phosphorylated SMAD3 (p‐SMAD3), and total SMAD2 in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334. (B) Quantification of p‐SMAD2, p‐SMAD3, and total SMAD2 protein expression levels. Densitometric values for p‐SMAD2, p‐SMAD3, and SMAD2 were normalized to GAPDH. (C, D) CCK‐8 assays measuring cell viability in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334 under the same 72 h assay conditions used in Figure . SB525334 was used at 10 μM as a selective ALK5/TGFβRI inhibitor. (E) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under the indicated treatment conditions; merged images are shown. (F) Quantification of cleaved caspase‐3 fluorescence intensity. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Figure Legend Snippet: ALK5/TGFβRI inhibition partially attenuates TTF‐associated SMAD phosphorylation, growth suppression, and cleaved caspase‐3 induction. (A) Western blot analysis of phosphorylated SMAD2 (p‐SMAD2), phosphorylated SMAD3 (p‐SMAD3), and total SMAD2 in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334. (B) Quantification of p‐SMAD2, p‐SMAD3, and total SMAD2 protein expression levels. Densitometric values for p‐SMAD2, p‐SMAD3, and SMAD2 were normalized to GAPDH. (C, D) CCK‐8 assays measuring cell viability in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334 under the same 72 h assay conditions used in Figure . SB525334 was used at 10 μM as a selective ALK5/TGFβRI inhibitor. (E) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under the indicated treatment conditions; merged images are shown. (F) Quantification of cleaved caspase‐3 fluorescence intensity. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Techniques Used: Inhibition, Phospho-proteomics, Western Blot, Analysis, Control, Expressing, CCK-8 Assay, Immunofluorescence, Staining, Fluorescence

Incubation:

Article Title: Trimethylamine N-oxide, a Gut Microbiota Metabolite, Promotes Diabetes-Mediated Erectile Dysfunction via a PANoptotic-Like Process Involving Pyroptosis, Apoptosis, and Necroptosis in CCSMCs.
Article Snippet: Background: Trimethylamine N-oxide (TMAO), a key metabolite derived from gut microbiota dysbiosis, is known to influence various diabetic vascular complications.. However, its specific role and the programmed cell death mechanisms underlying the development of diabetes-mediated erectile dysfunction (DMED) remain to be fully elucidated.. Objective: To investigate the mechanism by which TMAO mediates corpus cavernosum smooth muscle cell (CCSMC) dysfunction and promotes DMED in type 1 diabetic rats, with a focus on the involvement of the PI3K/Akt-regulated PANoptotic-like process.

Article Title: SC79 exerts neuroprotective effects in the model of experimental intracerebral hemorrhage.
Article Snippet: Intracerebral hemorrhage (ICH) is the most devastating subtype of stroke, yet specific treatments with conclusive clinical benefit remain lacking.. The protein kinase B (AKT) signaling pathway is essential to various cellular functions in stroke.. The present study used SC79, a specific AKT activator previously validated in ischemic stroke models, to explore therapeutic approaches for ICH in both in vivo and in vitro models.

Article Title: Hypoxia-induced exosomal CAMTA1 promotes radio-resistance in MDA-MB-231 cells by regulating NRG1 to mediate M2 macrophage polarization
Article Snippet: Briefly, antigen retrieval was performed by heating the tissue samples in 1X sodium citrate buffer using a microwave, followed by the incubation with 3% hydrogen peroxide for 10 min and subsequent inhibition with 3% normal goat serum (Solarbio, China) for 1 h at room temperature ( ). .. The slices were then incubated with primary antibody against NRG1 (cat. no. 83323-6-RR; 1:500; Proteintech Group, Inc.), CD163 (cat. no. 83285-4-RR; 1:2,000; Proteintech Group, Inc.) and Caspase-3 (cat. no. 19677-1-AP; 1:500; Proteintech Group, Inc.) overnight at 4°C. .. On the next day, the slices were incubated with HRP-labeled secondary antibody (cat. no. ab6721; 1:1,000; Abcam) for 1 h at room temperature.

Centrifugation:

BIA-KA:

Article Title: Glycyrrhizic Acid Relieves Fatigue Induced by Acute and Chronic Exercise in Mice via Inhibition of the NF‐κB/NLRP3 Signaling Pathway
Article Snippet: Gly‐A was provided by Chengdu Must Bio‐Technology Co. LTD. Nandrolone decanoate (Nandro) and TA were provided by Shanghai Macklin Technology Co., LTD. Formoterol fumarate (Formo) was provided by Shanghai Aladdin Biochemical Technology Co., LTD. SOD, MDA, L‐LDH, and CK assay kits were obtained from Beijing Solaibao Technology Co. LTD. .. The BCA protein assay kit and SDS‐PAGE gel kit were obtained from Shanghai Yisheng Biotechnology Co., LTD. Antibodies for iNOS, NLRP3, NF‐κB, Bax, Bcl‐2, Caspase 3, and GAPDH were obtained from Proteintech. .. Antibodies for Iba‐1 were obtained from FUJIFILM Wako Chemical Corporation.

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Journal: CNS Neuroscience & Therapeutics

doi: 10.1002/cns.71195

Figure Lengend Snippet: TMZ+TTF treatment enhances apoptotic responses in glioblastoma cells. (A) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under different treatment conditions. (B) Quantification of cleaved caspase‐3 fluorescence intensity. (C, E) Representative Annexin V‐FITC/PI flow cytometry plots showing the distribution of viable and apoptotic cell populations at 24 and 48 h in U251 and SHG140 cells, respectively. Lower left: Viable cells; lower right: Early apoptotic cells; upper right: Late apoptotic cells; upper left: PI‐positive non‐apoptotic/dead cells. (D, F) Quantitative analysis of viable‐cell fractions derived from Annexin V‐FITC/PI flow cytometry in U251 and SHG140 cells at 24 and 48 h. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. At least 10,000 events were acquired per flow‐cytometry sample. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test within each time point. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: For cleaved caspase‐3 immunofluorescence, cells were fixed with 4% paraformaldehyde, permeabilized with 0.5% Triton X‐100, blocked with 5% BSA, and incubated overnight at 4°C with anti‐cleaved caspase‐3 antibody (Proteintech, USA; Cat. No. 25546–1‐AP; 1:200).

Techniques: Immunofluorescence, Staining, Fluorescence, Flow Cytometry, Analysis, Derivative Assay

Journal: CNS Neuroscience & Therapeutics

doi: 10.1002/cns.71195

Figure Lengend Snippet: ALK5/TGFβRI inhibition partially attenuates TTF‐associated SMAD phosphorylation, growth suppression, and cleaved caspase‐3 induction. (A) Western blot analysis of phosphorylated SMAD2 (p‐SMAD2), phosphorylated SMAD3 (p‐SMAD3), and total SMAD2 in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334. (B) Quantification of p‐SMAD2, p‐SMAD3, and total SMAD2 protein expression levels. Densitometric values for p‐SMAD2, p‐SMAD3, and SMAD2 were normalized to GAPDH. (C, D) CCK‐8 assays measuring cell viability in U251 and SHG140 cells treated with vehicle control, TTF, SB525334, or TTF+SB525334 under the same 72 h assay conditions used in Figure . SB525334 was used at 10 μM as a selective ALK5/TGFβRI inhibitor. (E) Immunofluorescence staining of cleaved caspase‐3 (red) and nuclei (blue, DAPI) in U251 and SHG140 cells under the indicated treatment conditions; merged images are shown. (F) Quantification of cleaved caspase‐3 fluorescence intensity. For cleaved caspase‐3 quantification, three random 20× fields were averaged within each independent experiment. Data are presented as mean ± SD ( n = 3 independent experiments). Statistical analysis was performed using one‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Techniques: Inhibition, Phospho-proteomics, Western Blot, Analysis, Control, Expressing, CCK-8 Assay, Immunofluorescence, Staining, Fluorescence

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Images

1) Product Images from "Tumor Treating Fields Enhance Temozolomide‐Associated Growth Suppression in Glioblastoma Cells and Patient‐Derived Organoids Through Cell‐Cycle Blockade, Apoptosis, and SMAD ‐Associated Signaling"

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